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Conserved domains on  [gi|644359839|ref|WP_025303374|]
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MULTISPECIES: RidA family protein [Serratia]

Protein Classification

RidA family protein( domain architecture ID 10087367)

RidA (reactive intermediate/imine deaminase A) family protein similar to 2-aminomuconate deaminase that hydrolyzes 2-aminomuconate to 4-oxalocrotonate, and releases ammonia in the modified meta-cleavage pathway by forming various compounds including acetaldehyde, pyruvic acid, acetyl-CoA, and succinate, that may enter the Krebs cycle

EC:  3.5.-.-
Gene Ontology:  GO:0016787
PubMed:  22094463|25975565

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
16-121 1.22e-27

YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


:

Pssm-ID: 100004 [Multi-domain]  Cd Length: 107  Bit Score: 97.63  E-value: 1.22e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644359839  16 FSWATRGGGMLFTA-HGPVRADGSIDTGAPERQITLTFDNLAQTLKAAGSHSDKVLQVIVYLTDVNDVKCLDDIYRKYF- 93
Cdd:cd00448    1 YSQAVRVGNLVFVSgQIPLDPDGELVPGDIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMADFAAVNEVYDEFFg 80
                         90       100
                 ....*....|....*....|....*...
gi 644359839  94 NYPYPNRSTVIVEKLVvPGMKIEITVSA 121
Cdd:cd00448   81 EGPPPARTAVGVAALP-PGALVEIEAIA 107
 
Name Accession Description Interval E-value
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
16-121 1.22e-27

YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


Pssm-ID: 100004 [Multi-domain]  Cd Length: 107  Bit Score: 97.63  E-value: 1.22e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644359839  16 FSWATRGGGMLFTA-HGPVRADGSIDTGAPERQITLTFDNLAQTLKAAGSHSDKVLQVIVYLTDVNDVKCLDDIYRKYF- 93
Cdd:cd00448    1 YSQAVRVGNLVFVSgQIPLDPDGELVPGDIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMADFAAVNEVYDEFFg 80
                         90       100
                 ....*....|....*....|....*...
gi 644359839  94 NYPYPNRSTVIVEKLVvPGMKIEITVSA 121
Cdd:cd00448   81 EGPPPARTAVGVAALP-PGALVEIEAIA 107
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
1-121 8.40e-27

Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 family [Defense mechanisms]; Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 family is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 440021  Cd Length: 125  Bit Score: 96.02  E-value: 8.40e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644359839   1 MREIVDTGLPEIGQPFSWATRGGGMLFTA-HGPVRADGSIDTGAPERQITLTFDNLAQTLKAAGSHSDKVLQVIVYLTDV 79
Cdd:COG0251    2 TRELINPPAPAPIGPYSQAVRVGNLVFVSgQVPLDPDTGELGGDIEAQTRQVLENILAVLAAAGGSLDDVVKVTVYLTDM 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 644359839  80 NDVKCLDDIYRKYFNYPYPNRSTVIVEKLvVPGMKIEITVSA 121
Cdd:COG0251   82 ADFAAVNEVYAEYFGEGRPARTAVGVAAL-PKGALVEIEAIA 122
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
15-122 8.12e-19

Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein synthesis by cleavage of mRNA. Previously thought to inhibit protein synthesis initiation. This protein may also be involved in the regulation of purine biosynthesis. YjgF (renamed RidA) family members are enamine/imine deaminases. They hydrolyze reactive intermediates released by PLP-dependent enzymes, including threonine dehydratase. YjgF also prevents inhibition of transaminase B (IlvE) in Salmonella.


Pssm-ID: 426010  Cd Length: 117  Bit Score: 75.41  E-value: 8.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644359839   15 PFSWATRGGGMLFTA-HGPVRAD-GSIDTGAPERQITLTFDNLAQTLKAAGSHSDKVLQVIVYLTDVNDVKCLDDIYRKY 92
Cdd:pfam01042   8 PYSQAVKAGNLVYVSgQIPLDPDtGKLVEGDVAEQTRQVLENIKAVLAAAGASLSDVVKVTIFLADMNDFAEVNEVYAEY 87
                          90       100       110
                  ....*....|....*....|....*....|.
gi 644359839   93 F-NYPYPNRSTVIVeKLVVPGMKIEITVSAI 122
Cdd:pfam01042  88 FdADKAPARSAVGV-AALPLGALVEIEAIAV 117
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
12-122 1.05e-17

reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of protein synthesis intiation, then as an endoribonuclease active on single-stranded mRNA, endoribonuclease L-PSP. Members of this family, conserved in all domains of life and often with several members per bacterial genome, appear to catalyze a reaction that minimizes toxic by-products from reactions catalyzed by pyridoxal phosphate-dependent enzymes. [Cellular processes, Other]


Pssm-ID: 129116  Cd Length: 124  Bit Score: 72.71  E-value: 1.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644359839   12 IGqPFSWATRGGGMLFTAhGPVRAD---GSIDTGAPERQITLTFDNLAQTLKAAGSHSDKVLQVIVYLTDVNDVKCLDDI 88
Cdd:TIGR00004  13 IG-PYSQAVKVGNTVYVS-GQIPLDpstGELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTDLNDFAEVNEV 90
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 644359839   89 YRKYFNYPYPNRSTVIVEKLvvP-GMKIEITVSAI 122
Cdd:TIGR00004  91 YGQYFDEHYPARSAVQVAAL--PkGVLVEIEAIAV 123
PRK11401 PRK11401
enamine/imine deaminase;
1-122 2.58e-07

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 46.21  E-value: 2.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644359839   1 MREIVDTG-LPEIGQPFSWATRGGGMLFTA-HGPVRADGSIDTGAPERQITLTFDNLAQTLKAAGSHSDKVLQVIVYLTD 78
Cdd:PRK11401   1 MKKIIETQrAPGAIGPYVQGVDLGSMVFTSgQIPVCPQTGEIPADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITD 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 644359839  79 VNDVKCLDDIYRKYFN---YPYPNRSTVIVEKLvVPGMKIEITVSAI 122
Cdd:PRK11401  81 LNDFATINEVYKQFFDehqATYPTRSCVQVARL-PKDVKLEIEAIAV 126
 
Name Accession Description Interval E-value
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
16-121 1.22e-27

YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


Pssm-ID: 100004 [Multi-domain]  Cd Length: 107  Bit Score: 97.63  E-value: 1.22e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644359839  16 FSWATRGGGMLFTA-HGPVRADGSIDTGAPERQITLTFDNLAQTLKAAGSHSDKVLQVIVYLTDVNDVKCLDDIYRKYF- 93
Cdd:cd00448    1 YSQAVRVGNLVFVSgQIPLDPDGELVPGDIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMADFAAVNEVYDEFFg 80
                         90       100
                 ....*....|....*....|....*...
gi 644359839  94 NYPYPNRSTVIVEKLVvPGMKIEITVSA 121
Cdd:cd00448   81 EGPPPARTAVGVAALP-PGALVEIEAIA 107
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
1-121 8.40e-27

Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 family [Defense mechanisms]; Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 family is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 440021  Cd Length: 125  Bit Score: 96.02  E-value: 8.40e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644359839   1 MREIVDTGLPEIGQPFSWATRGGGMLFTA-HGPVRADGSIDTGAPERQITLTFDNLAQTLKAAGSHSDKVLQVIVYLTDV 79
Cdd:COG0251    2 TRELINPPAPAPIGPYSQAVRVGNLVFVSgQVPLDPDTGELGGDIEAQTRQVLENILAVLAAAGGSLDDVVKVTVYLTDM 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 644359839  80 NDVKCLDDIYRKYFNYPYPNRSTVIVEKLvVPGMKIEITVSA 121
Cdd:COG0251   82 ADFAAVNEVYAEYFGEGRPARTAVGVAAL-PKGALVEIEAIA 122
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
15-122 8.12e-19

Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein synthesis by cleavage of mRNA. Previously thought to inhibit protein synthesis initiation. This protein may also be involved in the regulation of purine biosynthesis. YjgF (renamed RidA) family members are enamine/imine deaminases. They hydrolyze reactive intermediates released by PLP-dependent enzymes, including threonine dehydratase. YjgF also prevents inhibition of transaminase B (IlvE) in Salmonella.


Pssm-ID: 426010  Cd Length: 117  Bit Score: 75.41  E-value: 8.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644359839   15 PFSWATRGGGMLFTA-HGPVRAD-GSIDTGAPERQITLTFDNLAQTLKAAGSHSDKVLQVIVYLTDVNDVKCLDDIYRKY 92
Cdd:pfam01042   8 PYSQAVKAGNLVYVSgQIPLDPDtGKLVEGDVAEQTRQVLENIKAVLAAAGASLSDVVKVTIFLADMNDFAEVNEVYAEY 87
                          90       100       110
                  ....*....|....*....|....*....|.
gi 644359839   93 F-NYPYPNRSTVIVeKLVVPGMKIEITVSAI 122
Cdd:pfam01042  88 FdADKAPARSAVGV-AALPLGALVEIEAIAV 117
YjgH_like cd02198
YjgH belongs to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, ...
16-123 5.72e-18

YjgH belongs to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


Pssm-ID: 100005  Cd Length: 111  Bit Score: 73.06  E-value: 5.72e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644359839  16 FSWATRGGGMLFTAhGPV--RADGSIDTGaPERQITLTFDNLAQTLKAAGSHSDKVLQVIVYLTDV-NDVKCLDDIYRKY 92
Cdd:cd02198    3 YSPAVRVGDTLFVS-GQVgsDADGSVAED-FEAQFRLAFQNLGAVLEAAGCSFDDVVELTTFHVDMaAHLPAFAAVKDEY 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 644359839  93 FNYPYPNRSTVIVEKLVVPGMKIEITVSAIA 123
Cdd:cd02198   81 FKEPYPAWTAVGVAWLARPGLLVEIKVVAVR 111
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
12-122 1.05e-17

reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of protein synthesis intiation, then as an endoribonuclease active on single-stranded mRNA, endoribonuclease L-PSP. Members of this family, conserved in all domains of life and often with several members per bacterial genome, appear to catalyze a reaction that minimizes toxic by-products from reactions catalyzed by pyridoxal phosphate-dependent enzymes. [Cellular processes, Other]


Pssm-ID: 129116  Cd Length: 124  Bit Score: 72.71  E-value: 1.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644359839   12 IGqPFSWATRGGGMLFTAhGPVRAD---GSIDTGAPERQITLTFDNLAQTLKAAGSHSDKVLQVIVYLTDVNDVKCLDDI 88
Cdd:TIGR00004  13 IG-PYSQAVKVGNTVYVS-GQIPLDpstGELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTDLNDFAEVNEV 90
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 644359839   89 YRKYFNYPYPNRSTVIVEKLvvP-GMKIEITVSAI 122
Cdd:TIGR00004  91 YGQYFDEHYPARSAVQVAAL--PkGVLVEIEAIAV 123
YjgF_YER057c_UK114_like_6 cd06154
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
16-121 2.74e-11

This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


Pssm-ID: 100011  Cd Length: 119  Bit Score: 56.02  E-value: 2.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644359839  16 FSWATRGGGMLFTAH-GPVRADGSIDTGAPERQITLTFDNLAQTLKAAGSHSDKVLQVIVYLTDVNDVKCLDDIYRKYFN 94
Cdd:cd06154   13 YSRAVRVGNWVFVSGtTGYDYDGMVMPGDAYEQTRQCLEIIEAALAEAGASLEDVVRTRMYVTDIADFEAVGRAHGEVFG 92
                         90       100
                 ....*....|....*....|....*..
gi 644359839  95 YPYPNRSTVIVEKLVVPGMKIEITVSA 121
Cdd:cd06154   93 DIRPAATMVVVSLLVDPEMLVEIEVTA 119
YjgF_YER057c_UK114_like_4 cd06152
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
45-122 3.59e-10

YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


Pssm-ID: 100009  Cd Length: 114  Bit Score: 53.08  E-value: 3.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644359839  45 ERQITLTFDNLAQTLKAAGSHS-DKVLQVIVYLTDVNDVKCLDDI---YRKYFnypyPNRS---TVI-VEKLVVPGMKIE 116
Cdd:cd06152   33 EEEIDQAFDNVELALKAAGGKGwEQVYKVNSYHVDIKNEEAFGLMvenFKKWM----PNHQpiwTCVgVTALGLPGMRVE 108

                 ....*.
gi 644359839 117 ITVSAI 122
Cdd:cd06152  109 IEVDAI 114
YjgF_YER057c_UK114_like_2 cd06150
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
23-121 7.43e-09

This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


Pssm-ID: 100007  Cd Length: 105  Bit Score: 49.46  E-value: 7.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644359839  23 GGMLFTAhGPVRADGSIDTGAPERQItltFDNLAQTLKAAGSHSDKVLQVIVYLTDVNDVKCLDDIYRKYF-NYPYPNRS 101
Cdd:cd06150   10 NGTVYLA-GQVADDTSADITGQTRQV---LAKIDALLAEAGSDKSRILSATIWLADMADFAAMNAVWDAWVpPGHAPARA 85
                         90       100
                 ....*....|....*....|
gi 644359839 102 TVIVeKLVVPGMKIEITVSA 121
Cdd:cd06150   86 CVEA-KLADPGYLVEIVVTA 104
PRK11401 PRK11401
enamine/imine deaminase;
1-122 2.58e-07

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 46.21  E-value: 2.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644359839   1 MREIVDTG-LPEIGQPFSWATRGGGMLFTA-HGPVRADGSIDTGAPERQITLTFDNLAQTLKAAGSHSDKVLQVIVYLTD 78
Cdd:PRK11401   1 MKKIIETQrAPGAIGPYVQGVDLGSMVFTSgQIPVCPQTGEIPADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITD 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 644359839  79 VNDVKCLDDIYRKYFN---YPYPNRSTVIVEKLvVPGMKIEITVSAI 122
Cdd:PRK11401  81 LNDFATINEVYKQFFDehqATYPTRSCVQVARL-PKDVKLEIEAIAV 126
YjgF_YER057c_UK114_like_5 cd06153
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
17-93 1.95e-06

This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


Pssm-ID: 100010  Cd Length: 114  Bit Score: 43.40  E-value: 1.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644359839  17 SWATRGGGMLF---TAhgPVRADGSIDTGAPERQITLTFDNLAQTLKAAG-----SHSDKVLQVIVYLTDVNDVKCLDDI 88
Cdd:cd06153    6 LLAAGGRTHLFisgTA--SIVGHGTVHPGDVEAQTRETLENIEALLEAAGrgggaQFLADLLRLKVYLRDREDLPAVRAI 83

                 ....*
gi 644359839  89 YRKYF 93
Cdd:cd06153   84 LAARL 88
YjgF_YER057c_UK114_like_3 cd06151
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
31-121 9.51e-05

This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


Pssm-ID: 100008  Cd Length: 126  Bit Score: 39.23  E-value: 9.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644359839  31 GPVRADGSIDT----GAPERQITLTFDNLAQTLKAAGSHSDKVLQVIVYLtdVNDVKCLDDI--------YRKYFNYP-- 96
Cdd:cd06151   22 AVVNASAPKGSparyGDTETQTISVLKRIETILQSQGLTMGDVVKMRVFL--VADPALDGKMdfagfmkaYRQFFGTAeq 99
                         90       100
                 ....*....|....*....|....*..
gi 644359839  97 --YPNRSTVIVEKLVVPGMKIEITVSA 121
Cdd:cd06151  100 pnKPARSTLQVAGLVNPGWLVEIEVVA 126
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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